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J. Biol. Chem., Vol. 279, Issue 31, 32046-32054, July 30, 2004
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From the
Howard Hughes Medical Institute and ¶Microchemistry and Proteomics Analysis Facility, Harvard University, Cambridge, Massachusetts 02138 and ||Department of Cell Biology and Physiology and **Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110-1093
14-3-3 proteins regulate the cell division cycle and play a pivotal role in blocking cell cycle advancement after activation of the DNA replication and DNA damage checkpoints. Here we describe a global proteomics analysis to identify proteins that bind to 14-3-3s during interphase and mitosis. 14-3-3-binding proteins were purified from extracts of interphase and mitotic HeLa cells using specific peptide elution from 14-3-3
affinity columns. Proteins that specifically bound and eluted from the affinity columns were identified by microcapillary high pressure liquid chromatography tandem mass spectrometry analysis. Several known and novel 14-3-3-interacting proteins were identified in this screen. Identified proteins are involved in cell cycle regulation, signaling, metabolism, protein synthesis, nucleic acid binding, chromatin structure, protein folding, proteolysis, nucleolar function, and nuclear transport as well as several other cellular processes. In some cases 14-3-3 binding was cell cycle-dependent, whereas in other cases the binding was shown to be cell cycle-independent. This study adds to the growing list of human 14-3-3-binding proteins and implicates a role for 14-3-3 proteins in a plethora of essential biological processes.
Received for publication, March 18, 2004 , and in revised form, May 12, 2004.
* This work was supported in part by a National Institutes of Health grant and a Siteman Cancer Center Research Development Award (to H. P.-W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains Supplemental Table 1.
An Associate of the Howard Hughes Medical Institute.
An Investigator of the Howard Hughes Medical Institute. To whom correspondence should be addressed. Tel.: 314-362-6812; Fax: 314-362-3709; E-mail: hpiwnica{at}cellbiology.wustl.edu.
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